X-ray diffraction
2.5Å resolution

PKR kinase domain- eIF2alpha- AMP-PNP complex.


Function and Biology Details

Reactions catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Eukaryotic translation initiation factor 2 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 20.55 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
  • Canonical: P20459 (Residues: 3-176; Coverage: 57%)
Gene names: J1429, SUI2, TIF211, YJR007W
Sequence domains: S1 RNA binding domain
Structure domains:
Interferon-induced, double-stranded RNA-activated protein kinase Chains: B, C
Molecule details ›
Chains: B, C
Length: 284 amino acids
Theoretical weight: 32.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P19525 (Residues: 258-551; Coverage: 51%)
Gene names: EIF2AK2, PKR, PRKR
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 64.659Å b: 48.75Å c: 133.434Å
α: 90° β: 98.44° γ: 90°
R R work R free
0.234 0.228 0.286
Expression system: Escherichia coli